Peptidase D (prolidase) (PEPD)

Peptidase D, also known as prolidase and encoded by the PEPD gene, is a ubiquitously expressed cytosolic metalloexopeptidase essential for the final step of collagen degradation and protein metabolism[1][2][5]. It uniquely cleaves dipeptides with C-terminal proline or hydroxyproline, releasing these amino acids for reuse in pathways including collagen synthesis, making it crucial for extracellular matrix remodeling, wound healing, and cellular proliferation[1][2][5]. Prolidase deficiency, an autosomal recessive disorder due to loss of function mutations, leads to a constellation of symptoms including skin ulcerations, mental retardation, and recurrent infections[1][2][5]. The enzyme is also under investigation as a disease biomarker and may participate in non-enzymatic cell regulatory roles[2].

Other names

prolidaseXaa-Pro dipeptidaseX-Pro dipeptidaseproline dipeptidaseimidodipeptidase

Enzyme inhibitors could theoretically reduce prolidase/prolidase D activity by chelating essential metal ions or binding the active site, but no clinically approved inhibitors are listed in the available literature